Biology:PIAS4
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
E3 SUMO-protein ligase PIAS4 is one of several protein inhibitor of activated STAT (PIAS) proteins. It is also known as a protein inhibitor of activated STAT protein gamma (PIASg or PIASy), and is an enzyme that in humans is encoded by the PIAS4 gene.[1][2]
Interactions
PIAS4 has been shown to interact with Mothers against decapentaplegic homolog 6,[3] Mothers against decapentaplegic homolog 7[3] and Lymphoid enhancer-binding factor 1.[4] PIAS4 has been shown to be responsible for the SUMOylation of inhibited Werner syndrome helicase (WRN) trapped on DNA in microsatellite unstable cancer cells. [5]
References
- ↑ "Inhibition of Stat1-mediated gene activation by PIAS1". Proc Natl Acad Sci U S A 95 (18): 10626–31. Sep 1998. doi:10.1073/pnas.95.18.10626. PMID 9724754. Bibcode: 1998PNAS...9510626L.
- ↑ "Entrez Gene: PIAS4 Protein inhibitor of activated STAT, 4". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=51588.
- ↑ 3.0 3.1 Imoto, Seiyu; Sugiyama Kenji; Muromoto Ryuta; Sato Noriko; Yamamoto Tetsuya; Matsuda Tadashi (Sep 2003). "Regulation of transforming growth factor-beta signaling by protein inhibitor of activated STAT, PIASy through Smad3". J. Biol. Chem. 278 (36): 34253–8. doi:10.1074/jbc.M304961200. ISSN 0021-9258. PMID 12815042.
- ↑ Sachdev, S; Bruhn L; Sieber H; Pichler A; Melchior F; Grosschedl R (Dec 2001). "PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies". Genes Dev. 15 (23): 3088–103. doi:10.1101/gad.944801. ISSN 0890-9369. PMID 11731474.
- ↑ "WRN inhibition leads to its chromatin-associated degradation via the PIAS4-RNF4-p97/VCP axis". Nat. Commun. 15 (6059). July 2024. doi:10.1038/s41467-024-50178-3. PMID 39025847. Bibcode: 2024NatCo..15.6059R.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "A transcriptional corepressor of Stat1 with an essential LXXLL signature motif". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3203–7. 2001. doi:10.1073/pnas.051489598. PMID 11248056. Bibcode: 2001PNAS...98.3203L.
- "A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis". Apoptosis 6 (3): 221–34. 2001. doi:10.1023/A:1011392811628. PMID 11388671.
- "Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells". Oncogene 20 (29): 3880–7. 2001. doi:10.1038/sj.onc.1204489. PMID 11439351.
- "PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies". Genes Dev. 15 (23): 3088–103. 2001. doi:10.1101/gad.944801. PMID 11731474.
- "Characterization of stage progression in chronic myeloid leukemia by DNA microarray with purified hematopoietic stem cells". Oncogene 20 (57): 8249–57. 2002. doi:10.1038/sj.onc.1205029. PMID 11781839.
- "Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators". J. Biol. Chem. 277 (19): 16993–7001. 2002. doi:10.1074/jbc.M109217200. PMID 11877418.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3". J. Biol. Chem. 278 (11): 9134–41. 2003. doi:10.1074/jbc.M210440200. PMID 12511558.
- "Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner". Eur. J. Biochem. 270 (6): 1338–48. 2003. doi:10.1046/j.1432-1033.2003.03504.x. PMID 12631292.
- "Sumoylation is involved in beta-catenin-dependent activation of Tcf-4". EMBO J. 22 (9): 2047–59. 2003. doi:10.1093/emboj/cdg204. PMID 12727872.
- "Sumoylation of Smad4, the common Smad mediator of transforming growth factor-beta family signaling". J. Biol. Chem. 278 (30): 27853–63. 2003. doi:10.1074/jbc.M301755200. PMID 12740389.
- "Modification of GATA-2 transcriptional activity in endothelial cells by the SUMO E3 ligase PIASy". Circ. Res. 92 (11): 1201–8. 2003. doi:10.1161/01.RES.0000076893.70898.36. PMID 12750312.
- "Regulation of transforming growth factor-beta signaling by protein inhibitor of activated STAT, PIASy through Smad3". J. Biol. Chem. 278 (36): 34253–8. 2003. doi:10.1074/jbc.M304961200. PMID 12815042.
- "PIASgamma represses the transcriptional activation induced by the nuclear receptor Nurr1". J. Biol. Chem. 279 (3): 2005–11. 2004. doi:10.1074/jbc.M308113200. PMID 14559918.
- "PIASy-mediated repression of the androgen receptor is independent of sumoylation". Oncogene 23 (17): 3059–66. 2004. doi:10.1038/sj.onc.1207443. PMID 14981544.
- "Convergence of interferon-gamma and progesterone signaling pathways in human endometrium: role of PIASy (protein inhibitor of activated signal transducer and activator of transcription-y)". Mol. Endocrinol. 18 (8): 1988–99. 2005. doi:10.1210/me.2003-0467. PMID 15155784.
- "The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway". Biochem. Biophys. Res. Commun. 319 (1): 275–82. 2004. doi:10.1016/j.bbrc.2004.04.161. PMID 15158472. Bibcode: 2004BBRC..319..275I.
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